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P2Y purinoceptor 12 (P2Y12) (ADP-glucose receptor) (ADPG-R) (P2T(AC)) (P2Y(AC)) (P2Y(cyc)) (P2Y12 platelet ADP receptor) (P2Y(ADP)) (SP1999)

 P2Y12_HUMAN             Reviewed;         342 AA.
Q9H244; D3DNJ5; Q546J7;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=P2Y purinoceptor 12;
Short=P2Y12;
AltName: Full=ADP-glucose receptor;
Short=ADPG-R;
AltName: Full=P2T(AC);
AltName: Full=P2Y(AC);
AltName: Full=P2Y(cyc);
AltName: Full=P2Y12 platelet ADP receptor;
Short=P2Y(ADP);
AltName: Full=SP1999;
Name=P2RY12; Synonyms=HORK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INVOLVEMENT IN BDPLT8.
PubMed=11196645; DOI=10.1038/35051599;
Hollopeter G., Jantzen H.-M., Vincent D., Li G., England L.,
Ramakrishnan V., Yang R.-B., Nurden P., Nurden A., Julius D.J.,
Conley P.B.;
"Identification of the platelet ADP receptor targeted by
antithrombotic drugs.";
Nature 409:202-207(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Hypothalamus;
PubMed=11104774; DOI=10.1074/jbc.M009718200;
Zhang F.L., Luo L., Gustafson E., Lachowicz J., Smith M., Qiao X.,
Liu Y.-H., Chen G., Pramanik B., Laz T.M., Palmer K., Bayne M.,
Monsma F.J. Jr.;
"ADP is the cognate ligand for the orphan G protein-coupled receptor
SP1999.";
J. Biol. Chem. 276:8608-8615(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11502873;
Takasaki J., Kamohara M., Saito T., Matsumoto M., Matsumoto S.,
Ohishi T., Soga T., Matsushime H., Furuichi K.;
"Molecular cloning of the platelet P2T(AC) ADP receptor:
pharmacological comparison with another ADP receptor, the P2Y1
receptor.";
Mol. Pharmacol. 60:432-439(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Reinscheid R.K., Nothacker H.-P., Wang Z., Zeng J., Ehlert F.J.,
Civelli O.;
"ADP-glucose activates a G-protein coupled receptor and inhibits
smooth muscle contractions.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
Bruess M., von Kugelgen I., Bonisch H.;
"Cloning and characterization of a human platelet ADP-receptor.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12044878; DOI=10.1016/S0014-5793(02)02775-8;
Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
"Identification of G protein-coupled receptor genes from the human
genome sequence.";
FEBS Lett. 520:97-101(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH THE AGONIST
AZD1283, FUNCTION, DISULFIDE BOND, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-80; SER-156; ASN-159; LYS-280 AND GLU-281.
PubMed=24670650; DOI=10.1038/nature13083;
Zhang K., Zhang J., Gao Z.G., Zhang D., Zhu L., Han G.W., Moss S.M.,
Paoletta S., Kiselev E., Lu W., Fenalti G., Zhang W., Mueller C.E.,
Yang H., Jiang H., Cherezov V., Katritch V., Jacobson K.A.,
Stevens R.C., Wu B., Zhao Q.;
"Structure of the human P2Y12 receptor in complex with an
antithrombotic drug.";
Nature 509:115-118(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-342 IN COMPLEX WITH THE
ADP ANALOG 2-(METHYLSULFANYL)ADENOSINE 5'-(TRIHYDROGEN DIPHOSPHATE),
FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF
SER-83; CYS-97; CYS-175; ARG-256 AND LYS-280.
PubMed=24784220; DOI=10.1038/nature13288;
Zhang J., Zhang K., Gao Z.G., Paoletta S., Zhang D., Han G.W., Li T.,
Ma L., Zhang W., Mueller C.E., Yang H., Jiang H., Cherezov V.,
Katritch V., Jacobson K.A., Stevens R.C., Wu B., Zhao Q.;
"Agonist-bound structure of the human P2Y12 receptor.";
Nature 509:119-122(2014).
[12]
VARIANTS BDPLT8 GLN-256 AND TRP-265, INVOLVEMENT IN BDPLT8, FUNCTION,
AND SUBCELLULAR LOCATION.
PubMed=12578987; DOI=10.1073/pnas.0437879100;
Cattaneo M., Zighetti M.L., Lombardi R., Martinez C., Lecchi A.,
Conley P.B., Ware J., Ruggeri Z.M.;
"Molecular bases of defective signal transduction in the platelet
P2Y12 receptor of a patient with congenital bleeding.";
Proc. Natl. Acad. Sci. U.S.A. 100:1978-1983(2003).
[13]
VARIANT BDPLT8 GLN-187.
PubMed=25428217; DOI=10.1182/blood-2013-07-517896;
Lecchi A., Razzari C., Paoletta S., Dupuis A., Nakamura L.,
Ohlmann P., Gachet C., Jacobson K.A., Zieger B., Cattaneo M.;
"Identification of a new dysfunctional platelet P2Y12 receptor variant
associated with bleeding diathesis.";
Blood 125:1006-1013(2015).
-!- FUNCTION: Receptor for ADP and ATP coupled to G-proteins that
inhibit the adenylyl cyclase second messenger system. Not
activated by UDP and UTP. Required for normal platelet aggregation
and blood coagulation. {ECO:0000269|PubMed:11104774,
ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:11502873,
ECO:0000269|PubMed:12578987, ECO:0000269|PubMed:24670650,
ECO:0000269|PubMed:24784220}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11196645,
ECO:0000269|PubMed:12578987, ECO:0000269|PubMed:24670650,
ECO:0000269|PubMed:24784220}; Multi-pass membrane protein
{ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:12578987,
ECO:0000269|PubMed:24670650, ECO:0000269|PubMed:24784220}.
-!- TISSUE SPECIFICITY: Highly expressed in the platelets, lower
levels in the brain. Lowest levels in the lung, appendix,
pituitary and adrenal gland. Expressed in the spinal cord and in
the fetal brain. {ECO:0000269|PubMed:11104774,
ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:11502873}.
-!- DOMAIN: The transmembrane domain is composed of seven
transmembrane helices; most of these are not strictly
perpendicular to the plane of the membrane, but are tilted and/or
kinked. Agonist binding promotes a conformation change in the
extracellular loops that leads to an inward movement of the
transmembrane helices. Antagonists such as AZD1283 can bind to an
overlapping site, but block the inward movement of the
transmembrane helices (PubMed:24670650, PubMed:24784220).
{ECO:0000269|PubMed:24670650, ECO:0000269|PubMed:24784220}.
-!- DISEASE: Bleeding disorder, platelet-type 8 (BDPLT8) [MIM:609821]:
A condition characterized by mild to moderate mucocutaneous
bleeding, and excessive bleeding after surgery or trauma. The
defect is due to severe impairment of platelet response to ADP
resulting in defective platelet aggregation.
{ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:12578987,
ECO:0000269|PubMed:25428217}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AF313449; AAG48944.1; -; mRNA.
EMBL; AF321815; AAK00948.1; -; mRNA.
EMBL; AB052684; BAB60824.1; -; mRNA.
EMBL; AF310685; AAL32292.1; -; Genomic_DNA.
EMBL; AJ320495; CAC87144.1; -; mRNA.
EMBL; AB083596; BAB89309.1; -; Genomic_DNA.
EMBL; AY136754; AAN01280.1; -; mRNA.
EMBL; CH471052; EAW78803.1; -; Genomic_DNA.
EMBL; CH471052; EAW78804.1; -; Genomic_DNA.
EMBL; BC017898; AAH17898.1; -; mRNA.
CCDS; CCDS3159.1; -.
RefSeq; NP_073625.1; NM_022788.4.
RefSeq; NP_795345.1; NM_176876.2.
RefSeq; XP_016862558.1; XM_017007069.1.
UniGene; Hs.591281; -.
UniGene; Hs.665544; -.
PDB; 1T78; Model; -; A=1-337.
PDB; 1VZ1; Model; -; A=1-337.
PDB; 1Y9C; Model; -; A=1-342.
PDB; 4NTJ; X-ray; 2.62 A; A=2-342.
PDB; 4PXZ; X-ray; 2.50 A; A=2-342.
PDB; 4PY0; X-ray; 3.10 A; A=2-342.
PDBsum; 1T78; -.
PDBsum; 1VZ1; -.
PDBsum; 1Y9C; -.
PDBsum; 4NTJ; -.
PDBsum; 4PXZ; -.
PDBsum; 4PY0; -.
ProteinModelPortal; Q9H244; -.
SMR; Q9H244; -.
BioGrid; 122309; 62.
DIP; DIP-61226N; -.
STRING; 9606.ENSP00000307259; -.
BindingDB; Q9H244; -.
ChEMBL; CHEMBL2001; -.
DrugBank; DB04902; AZD6140.
DrugBank; DB06441; Cangrelor.
DrugBank; DB00758; Clopidogrel.
DrugBank; DB01240; Epoprostenol.
DrugBank; DB06209; Prasugrel.
DrugBank; DB08816; Ticagrelor.
DrugBank; DB00208; Ticlopidine.
DrugBank; DB00374; Treprostinil.
GuidetoPHARMACOLOGY; 328; -.
iPTMnet; Q9H244; -.
PhosphoSitePlus; Q9H244; -.
DMDM; 21263835; -.
PaxDb; Q9H244; -.
PeptideAtlas; Q9H244; -.
PRIDE; Q9H244; -.
DNASU; 64805; -.
Ensembl; ENST00000302632; ENSP00000307259; ENSG00000169313.
GeneID; 64805; -.
KEGG; hsa:64805; -.
UCSC; uc003eyx.3; human.
CTD; 64805; -.
DisGeNET; 64805; -.
EuPathDB; HostDB:ENSG00000169313.9; -.
GeneCards; P2RY12; -.
HGNC; HGNC:18124; P2RY12.
HPA; HPA013796; -.
HPA; HPA014518; -.
MalaCards; P2RY12; -.
MIM; 600515; gene.
MIM; 609821; phenotype.
neXtProt; NX_Q9H244; -.
OpenTargets; ENSG00000169313; -.
Orphanet; 36355; P2Y12 defect.
Orphanet; 240935; Resistance to clopidogrel.
PharmGKB; PA134971947; -.
eggNOG; ENOG410IFYD; Eukaryota.
eggNOG; ENOG410ZJD1; LUCA.
GeneTree; ENSGT00640000091213; -.
HOGENOM; HOG000273884; -.
HOVERGEN; HBG108228; -.
InParanoid; Q9H244; -.
KO; K04298; -.
OMA; IKVFIII; -.
OrthoDB; EOG091G0B3H; -.
PhylomeDB; Q9H244; -.
TreeFam; TF330969; -.
Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
Reactome; R-HSA-417957; P2Y receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
GeneWiki; P2Y12; -.
GenomeRNAi; 64805; -.
PRO; PR:Q9H244; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000169313; -.
CleanEx; HS_P2RY12; -.
Genevisible; Q9H244; HS.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0001621; F:ADP receptor activity; IDA:UniProtKB.
GO; GO:0001609; F:G-protein coupled adenosine receptor activity; IEA:Ensembl.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
GO; GO:0071318; P:cellular response to ATP; ISS:ParkinsonsUK-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0008347; P:glial cell migration; IEA:Ensembl.
GO; GO:0007599; P:hemostasis; NAS:UniProtKB.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0010700; P:negative regulation of norepinephrine secretion; IEA:Ensembl.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0043270; P:positive regulation of ion transport; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IEA:Ensembl.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
GO; GO:1904139; P:regulation of microglial cell migration; ISS:ParkinsonsUK-UCL.
GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:ParkinsonsUK-UCL.
CDD; cd15150; 7tmA_P2Y12; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR005394; P2Y12_rcpt.
PANTHER; PTHR24233:SF0; PTHR24233:SF0; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01569; P2Y12PRNCPTR.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Hemostasis; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 342 P2Y purinoceptor 12.
/FTId=PRO_0000070036.
TOPO_DOM 1 27 Extracellular.
TRANSMEM 28 50 Helical; Name=1.
TOPO_DOM 51 61 Cytoplasmic.
TRANSMEM 62 82 Helical; Name=2.
TOPO_DOM 83 97 Extracellular.
TRANSMEM 98 118 Helical; Name=3.
TOPO_DOM 119 142 Cytoplasmic.
TRANSMEM 143 162 Helical; Name=4.
TOPO_DOM 163 185 Extracellular.
TRANSMEM 186 207 Helical; Name=5.
TOPO_DOM 208 233 Cytoplasmic.
TRANSMEM 234 259 Helical; Name=6.
TOPO_DOM 260 278 Extracellular.
TRANSMEM 279 298 Helical; Name=7.
TOPO_DOM 299 342 Cytoplasmic.
NP_BIND 156 159 ADP.
NP_BIND 175 179 ADP.
NP_BIND 256 259 ADP.
BINDING 93 93 ADP.
BINDING 97 97 ADP; via carbonyl oxygen.
BINDING 105 105 ADP.
BINDING 187 187 ADP.
BINDING 191 191 ADP.
BINDING 263 263 ADP.
BINDING 280 280 ADP.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPX4}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPX4}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 13 13 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 17 270
DISULFID 97 175
VARIANT 187 187 H -> Q (in BDPLT8).
{ECO:0000269|PubMed:25428217}.
/FTId=VAR_072802.
VARIANT 256 256 R -> Q (in BDPLT8; dbSNP:rs121917885).
{ECO:0000269|PubMed:12578987}.
/FTId=VAR_025383.
VARIANT 265 265 R -> W (in BDPLT8; dbSNP:rs121917886).
{ECO:0000269|PubMed:12578987}.
/FTId=VAR_025384.
VARIANT 330 330 E -> G (in dbSNP:rs16846673).
/FTId=VAR_049431.
MUTAGEN 80 80 K->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24670650}.
MUTAGEN 83 83 S->A: No effect on ADP binding.
{ECO:0000269|PubMed:24784220}.
MUTAGEN 97 97 C->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24784220}.
MUTAGEN 156 156 S->A: Slightly decreases affinity for
ADP. {ECO:0000269|PubMed:24670650}.
MUTAGEN 159 159 N->A: Slightly decreases affinity for
ADP. {ECO:0000269|PubMed:24670650}.
MUTAGEN 175 175 C->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24784220}.
MUTAGEN 256 256 R->A: Decreases affinity for ADP.
{ECO:0000269|PubMed:24784220}.
MUTAGEN 280 280 K->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24670650,
ECO:0000269|PubMed:24784220}.
MUTAGEN 281 281 E->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24670650}.
HELIX 24 50 {ECO:0000244|PDB:4PXZ}.
HELIX 58 74 {ECO:0000244|PDB:4PXZ}.
HELIX 77 85 {ECO:0000244|PDB:4PXZ}.
STRAND 86 88 {ECO:0000244|PDB:4PXZ}.
HELIX 91 98 {ECO:0000244|PDB:4PXZ}.
HELIX 100 127 {ECO:0000244|PDB:4PXZ}.
HELIX 136 161 {ECO:0000244|PDB:4PXZ}.
HELIX 175 178 {ECO:0000244|PDB:4PXZ}.
HELIX 181 226 {ECO:0000244|PDB:4PXZ}.
HELIX 231 233 {ECO:0000244|PDB:4PXZ}.
HELIX 236 248 {ECO:0000244|PDB:4PXZ}.
HELIX 250 264 {ECO:0000244|PDB:4PXZ}.
HELIX 270 293 {ECO:0000244|PDB:4PXZ}.
HELIX 296 299 {ECO:0000244|PDB:4PXZ}.
TURN 302 304 {ECO:0000244|PDB:4PXZ}.
SEQUENCE 342 AA; 39439 MW; 8553D2746C89176D CRC64;
MQAVDNLTSA PGNTSLCTRD YKITQVLFPL LYTVLFFVGL ITNGLAMRIF FQIRSKSNFI
IFLKNTVISD LLMILTFPFK ILSDAKLGTG PLRTFVCQVT SVIFYFTMYI SISFLGLITI
DRYQKTTRPF KTSNPKNLLG AKILSVVIWA FMFLLSLPNM ILTNRQPRDK NVKKCSFLKS
EFGLVWHEIV NYICQVIFWI NFLIVIVCYT LITKELYRSY VRTRGVGKVP RKKVNVKVFI
IIAVFFICFV PFHFARIPYT LSQTRDVFDC TAENTLFYVK ESTLWLTSLN ACLDPFIYFF
LCKSFRNSLI SMLKCPNSAT SLSQDNRKKE QDGGDPNEET PM


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